EP1034277B1 - Extrazelluläre Matrix-bindende Proteine von Staphylococcus aureus - Google Patents
Extrazelluläre Matrix-bindende Proteine von Staphylococcus aureus Download PDFInfo
- Publication number
- EP1034277B1 EP1034277B1 EP98959613A EP98959613A EP1034277B1 EP 1034277 B1 EP1034277 B1 EP 1034277B1 EP 98959613 A EP98959613 A EP 98959613A EP 98959613 A EP98959613 A EP 98959613A EP 1034277 B1 EP1034277 B1 EP 1034277B1
- Authority
- EP
- European Patent Office
- Prior art keywords
- clfb
- protein
- aureus
- proteins
- binding
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 108091009712 extracellular matrix binding proteins Proteins 0.000 title claims abstract description 17
- 102000033737 extracellular matrix binding proteins Human genes 0.000 title claims abstract description 17
- 241000191967 Staphylococcus aureus Species 0.000 title description 26
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 209
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 181
- 150000007523 nucleic acids Chemical group 0.000 claims abstract description 72
- 230000027455 binding Effects 0.000 claims abstract description 70
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 67
- 239000012634 fragment Substances 0.000 claims abstract description 57
- 208000015181 infectious disease Diseases 0.000 claims abstract description 39
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 claims abstract description 24
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 claims abstract description 24
- 239000003446 ligand Substances 0.000 claims abstract description 13
- 238000011282 treatment Methods 0.000 claims abstract description 13
- 150000001768 cations Chemical class 0.000 claims abstract description 9
- 210000002744 extracellular matrix Anatomy 0.000 claims abstract description 9
- 230000001419 dependent effect Effects 0.000 claims abstract description 8
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims abstract description 7
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims abstract description 7
- 102000039446 nucleic acids Human genes 0.000 claims description 41
- 108020004707 nucleic acids Proteins 0.000 claims description 41
- 238000000034 method Methods 0.000 claims description 38
- 229960005486 vaccine Drugs 0.000 claims description 21
- 239000000203 mixture Substances 0.000 claims description 16
- 239000013598 vector Substances 0.000 claims description 15
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 14
- 206010014665 endocarditis Diseases 0.000 claims description 9
- 239000008194 pharmaceutical composition Substances 0.000 claims description 9
- 210000003709 heart valve Anatomy 0.000 claims description 8
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 6
- 101710128530 Fibrinogen-binding protein Proteins 0.000 claims description 6
- 102000025748 fibrinogen binding proteins Human genes 0.000 claims description 6
- 230000002792 vascular Effects 0.000 claims description 6
- 238000009007 Diagnostic Kit Methods 0.000 claims description 4
- 230000000747 cardiac effect Effects 0.000 claims description 4
- 239000003937 drug carrier Substances 0.000 claims description 4
- 238000001990 intravenous administration Methods 0.000 claims description 4
- 239000007790 solid phase Substances 0.000 claims description 4
- 206010031252 Osteomyelitis Diseases 0.000 claims description 3
- 206010040047 Sepsis Diseases 0.000 claims description 3
- 244000005700 microbiome Species 0.000 claims description 3
- 239000011248 coating agent Substances 0.000 claims description 2
- 238000000576 coating method Methods 0.000 claims description 2
- 208000004396 mastitis Diseases 0.000 claims description 2
- 208000013223 septicemia Diseases 0.000 claims description 2
- 229940012952 fibrinogen Drugs 0.000 abstract description 98
- 102000008946 Fibrinogen Human genes 0.000 abstract description 94
- 108010049003 Fibrinogen Proteins 0.000 abstract description 93
- 108090000765 processed proteins & peptides Proteins 0.000 abstract description 45
- 150000001413 amino acids Chemical class 0.000 abstract description 34
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 34
- 230000000890 antigenic effect Effects 0.000 abstract description 15
- 208000027418 Wounds and injury Diseases 0.000 abstract description 12
- 238000011160 research Methods 0.000 abstract description 12
- 206010052428 Wound Diseases 0.000 abstract description 11
- 239000012620 biological material Substances 0.000 abstract description 9
- 238000003745 diagnosis Methods 0.000 abstract description 9
- 230000005764 inhibitory process Effects 0.000 abstract description 8
- 230000002265 prevention Effects 0.000 abstract description 8
- 101000743092 Bacillus spizizenii (strain DSM 15029 / JCM 12233 / NBRC 101239 / NRRL B-23049 / TU-B-10) tRNA3(Ser)-specific nuclease WapA Proteins 0.000 abstract description 6
- 101000743093 Bacillus subtilis subsp. natto (strain BEST195) tRNA(Glu)-specific nuclease WapA Proteins 0.000 abstract description 6
- 239000002981 blocking agent Substances 0.000 abstract description 5
- 108010076504 Protein Sorting Signals Proteins 0.000 description 135
- 101150035844 clfB gene Proteins 0.000 description 71
- 108020004414 DNA Proteins 0.000 description 54
- 210000004027 cell Anatomy 0.000 description 51
- 239000000523 sample Substances 0.000 description 50
- 229940024606 amino acid Drugs 0.000 description 33
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 32
- 239000002953 phosphate buffered saline Substances 0.000 description 32
- 239000013612 plasmid Substances 0.000 description 31
- 238000003556 assay Methods 0.000 description 26
- 101150085107 clfA gene Proteins 0.000 description 23
- 239000000126 substance Substances 0.000 description 21
- 241000283973 Oryctolagus cuniculus Species 0.000 description 20
- 241000699670 Mus sp. Species 0.000 description 18
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 17
- 239000000427 antigen Substances 0.000 description 17
- 108091007433 antigens Proteins 0.000 description 17
- 102000036639 antigens Human genes 0.000 description 17
- 229940098773 bovine serum albumin Drugs 0.000 description 17
- 230000001580 bacterial effect Effects 0.000 description 16
- 230000000694 effects Effects 0.000 description 16
- 239000000047 product Substances 0.000 description 16
- 238000001514 detection method Methods 0.000 description 14
- 241000588724 Escherichia coli Species 0.000 description 13
- 230000014509 gene expression Effects 0.000 description 13
- 238000003752 polymerase chain reaction Methods 0.000 description 13
- 238000001262 western blot Methods 0.000 description 13
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 12
- 241001465754 Metazoa Species 0.000 description 12
- 238000004519 manufacturing process Methods 0.000 description 12
- 239000012071 phase Substances 0.000 description 12
- 238000012163 sequencing technique Methods 0.000 description 12
- 108010028750 Integrin-Binding Sialoprotein Proteins 0.000 description 11
- 102000016921 Integrin-Binding Sialoprotein Human genes 0.000 description 11
- 239000012528 membrane Substances 0.000 description 11
- 102000004190 Enzymes Human genes 0.000 description 10
- 108090000790 Enzymes Proteins 0.000 description 10
- 108700026244 Open Reading Frames Proteins 0.000 description 10
- 239000002671 adjuvant Substances 0.000 description 10
- 238000010367 cloning Methods 0.000 description 10
- 229940088598 enzyme Drugs 0.000 description 10
- 230000003993 interaction Effects 0.000 description 10
- 210000004899 c-terminal region Anatomy 0.000 description 9
- 238000006243 chemical reaction Methods 0.000 description 9
- 238000010790 dilution Methods 0.000 description 9
- 239000012895 dilution Substances 0.000 description 9
- 230000035772 mutation Effects 0.000 description 9
- 101150064504 sdrC gene Proteins 0.000 description 9
- 101150009625 sdrD gene Proteins 0.000 description 9
- 241000894006 Bacteria Species 0.000 description 8
- 238000002105 Southern blotting Methods 0.000 description 8
- 238000004873 anchoring Methods 0.000 description 8
- 238000002474 experimental method Methods 0.000 description 8
- 238000009396 hybridization Methods 0.000 description 8
- 230000003053 immunization Effects 0.000 description 8
- 238000002649 immunization Methods 0.000 description 8
- 230000002163 immunogen Effects 0.000 description 8
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 8
- 108010065152 Coagulase Proteins 0.000 description 7
- 108020004705 Codon Proteins 0.000 description 7
- 229920001213 Polysorbate 20 Polymers 0.000 description 7
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 7
- 108010031318 Vitronectin Proteins 0.000 description 7
- 102100035140 Vitronectin Human genes 0.000 description 7
- 210000004369 blood Anatomy 0.000 description 7
- 239000008280 blood Substances 0.000 description 7
- 239000003153 chemical reaction reagent Substances 0.000 description 7
- 238000012217 deletion Methods 0.000 description 7
- 230000037430 deletion Effects 0.000 description 7
- 229950003499 fibrin Drugs 0.000 description 7
- 229940106780 human fibrinogen Drugs 0.000 description 7
- 238000000338 in vitro Methods 0.000 description 7
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 7
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 7
- 101150073644 sdrE gene Proteins 0.000 description 7
- 238000006467 substitution reaction Methods 0.000 description 7
- 239000000758 substrate Substances 0.000 description 7
- 102000004237 Decorin Human genes 0.000 description 6
- 108090000738 Decorin Proteins 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 108010088842 Fibrinolysin Proteins 0.000 description 6
- 102000018697 Membrane Proteins Human genes 0.000 description 6
- 108010052285 Membrane Proteins Proteins 0.000 description 6
- 238000001042 affinity chromatography Methods 0.000 description 6
- -1 antibodies Proteins 0.000 description 6
- 239000000872 buffer Substances 0.000 description 6
- 238000003776 cleavage reaction Methods 0.000 description 6
- 239000000499 gel Substances 0.000 description 6
- 230000036039 immunity Effects 0.000 description 6
- 239000007924 injection Substances 0.000 description 6
- 238000002347 injection Methods 0.000 description 6
- 239000006166 lysate Substances 0.000 description 6
- 229910001629 magnesium chloride Inorganic materials 0.000 description 6
- 229940012957 plasmin Drugs 0.000 description 6
- 229920003229 poly(methyl methacrylate) Polymers 0.000 description 6
- 239000004926 polymethyl methacrylate Substances 0.000 description 6
- 229920001184 polypeptide Polymers 0.000 description 6
- 230000002829 reductive effect Effects 0.000 description 6
- 230000007017 scission Effects 0.000 description 6
- 238000012216 screening Methods 0.000 description 6
- 238000012807 shake-flask culturing Methods 0.000 description 6
- 238000012360 testing method Methods 0.000 description 6
- 238000011144 upstream manufacturing Methods 0.000 description 6
- 108010067306 Fibronectins Proteins 0.000 description 5
- 102000016359 Fibronectins Human genes 0.000 description 5
- 230000005526 G1 to G0 transition Effects 0.000 description 5
- 241000282412 Homo Species 0.000 description 5
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 5
- 108090000988 Lysostaphin Proteins 0.000 description 5
- 229920002684 Sepharose Polymers 0.000 description 5
- 208000007536 Thrombosis Diseases 0.000 description 5
- 230000003321 amplification Effects 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 230000037396 body weight Effects 0.000 description 5
- 230000008859 change Effects 0.000 description 5
- 230000000295 complement effect Effects 0.000 description 5
- 238000011161 development Methods 0.000 description 5
- 239000013604 expression vector Substances 0.000 description 5
- 238000001727 in vivo Methods 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 102000006495 integrins Human genes 0.000 description 5
- 108010044426 integrins Proteins 0.000 description 5
- 238000003199 nucleic acid amplification method Methods 0.000 description 5
- 239000002773 nucleotide Substances 0.000 description 5
- 125000003729 nucleotide group Chemical group 0.000 description 5
- 229920000642 polymer Polymers 0.000 description 5
- 238000002560 therapeutic procedure Methods 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 4
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 4
- 108700028369 Alleles Proteins 0.000 description 4
- 108090001008 Avidin Proteins 0.000 description 4
- 208000035143 Bacterial infection Diseases 0.000 description 4
- 102000014914 Carrier Proteins Human genes 0.000 description 4
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 4
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 4
- 108010073385 Fibrin Proteins 0.000 description 4
- 102000009123 Fibrin Human genes 0.000 description 4
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 4
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 4
- PXHVJJICTQNCMI-UHFFFAOYSA-N Nickel Chemical compound [Ni] PXHVJJICTQNCMI-UHFFFAOYSA-N 0.000 description 4
- 239000000020 Nitrocellulose Substances 0.000 description 4
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 4
- 108091081024 Start codon Proteins 0.000 description 4
- 108090000190 Thrombin Proteins 0.000 description 4
- 238000002835 absorbance Methods 0.000 description 4
- 239000008186 active pharmaceutical agent Substances 0.000 description 4
- 239000005557 antagonist Substances 0.000 description 4
- 208000022362 bacterial infectious disease Diseases 0.000 description 4
- 108091008324 binding proteins Proteins 0.000 description 4
- 210000002421 cell wall Anatomy 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 230000002950 deficient Effects 0.000 description 4
- 239000010432 diamond Substances 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 108020001507 fusion proteins Proteins 0.000 description 4
- 102000037865 fusion proteins Human genes 0.000 description 4
- 238000001631 haemodialysis Methods 0.000 description 4
- 230000028993 immune response Effects 0.000 description 4
- 239000007943 implant Substances 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 238000002372 labelling Methods 0.000 description 4
- 230000007246 mechanism Effects 0.000 description 4
- 229920001220 nitrocellulos Polymers 0.000 description 4
- 230000002018 overexpression Effects 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 210000001938 protoplast Anatomy 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 229960004072 thrombin Drugs 0.000 description 4
- 238000013519 translation Methods 0.000 description 4
- 230000007923 virulence factor Effects 0.000 description 4
- 239000000304 virulence factor Substances 0.000 description 4
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 3
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 3
- 102000004506 Blood Proteins Human genes 0.000 description 3
- 108010017384 Blood Proteins Proteins 0.000 description 3
- 238000002965 ELISA Methods 0.000 description 3
- ULGZDMOVFRHVEP-RWJQBGPGSA-N Erythromycin Chemical compound O([C@@H]1[C@@H](C)C(=O)O[C@@H]([C@@]([C@H](O)[C@@H](C)C(=O)[C@H](C)C[C@@](C)(O)[C@H](O[C@H]2[C@@H]([C@H](C[C@@H](C)O2)N(C)C)O)[C@H]1C)(C)O)CC)[C@H]1C[C@@](C)(OC)[C@@H](O)[C@H](C)O1 ULGZDMOVFRHVEP-RWJQBGPGSA-N 0.000 description 3
- 241000192125 Firmicutes Species 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- RJQXTJLFIWVMTO-TYNCELHUSA-N Methicillin Chemical compound COC1=CC=CC(OC)=C1C(=O)N[C@@H]1C(=O)N2[C@@H](C(O)=O)C(C)(C)S[C@@H]21 RJQXTJLFIWVMTO-TYNCELHUSA-N 0.000 description 3
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010090804 Streptavidin Proteins 0.000 description 3
- 210000001744 T-lymphocyte Anatomy 0.000 description 3
- 239000003242 anti bacterial agent Substances 0.000 description 3
- 230000000844 anti-bacterial effect Effects 0.000 description 3
- 229940088710 antibiotic agent Drugs 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 229960002685 biotin Drugs 0.000 description 3
- 239000011616 biotin Substances 0.000 description 3
- YXVFYQXJAXKLAK-UHFFFAOYSA-N biphenyl-4-ol Chemical group C1=CC(O)=CC=C1C1=CC=CC=C1 YXVFYQXJAXKLAK-UHFFFAOYSA-N 0.000 description 3
- 210000000988 bone and bone Anatomy 0.000 description 3
- 239000000969 carrier Substances 0.000 description 3
- 230000007969 cellular immunity Effects 0.000 description 3
- 238000013270 controlled release Methods 0.000 description 3
- 230000007423 decrease Effects 0.000 description 3
- 238000004925 denaturation Methods 0.000 description 3
- 230000036425 denaturation Effects 0.000 description 3
- 238000005538 encapsulation Methods 0.000 description 3
- 235000013861 fat-free Nutrition 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 108010037896 heparin-binding hemagglutinin Proteins 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 238000003018 immunoassay Methods 0.000 description 3
- 230000000977 initiatory effect Effects 0.000 description 3
- 239000002054 inoculum Substances 0.000 description 3
- 238000007912 intraperitoneal administration Methods 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 3
- 210000003734 kidney Anatomy 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 229910052751 metal Inorganic materials 0.000 description 3
- 239000002184 metal Substances 0.000 description 3
- 229960003085 meticillin Drugs 0.000 description 3
- 235000013336 milk Nutrition 0.000 description 3
- 239000008267 milk Substances 0.000 description 3
- 210000004080 milk Anatomy 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 239000002853 nucleic acid probe Substances 0.000 description 3
- 230000008520 organization Effects 0.000 description 3
- 239000004033 plastic Substances 0.000 description 3
- 229920003023 plastic Polymers 0.000 description 3
- 238000011533 pre-incubation Methods 0.000 description 3
- 239000003755 preservative agent Substances 0.000 description 3
- 230000002441 reversible effect Effects 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- 238000010361 transduction Methods 0.000 description 3
- 230000026683 transduction Effects 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 238000009631 Broth culture Methods 0.000 description 2
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 2
- 241000282465 Canis Species 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- 108010035532 Collagen Proteins 0.000 description 2
- 102000008186 Collagen Human genes 0.000 description 2
- 238000001712 DNA sequencing Methods 0.000 description 2
- 108010016626 Dipeptides Proteins 0.000 description 2
- 241000701959 Escherichia virus Lambda Species 0.000 description 2
- 102100024783 Fibrinogen gamma chain Human genes 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- 229910021380 Manganese Chloride Inorganic materials 0.000 description 2
- GLFNIEUTAYBVOC-UHFFFAOYSA-L Manganese chloride Chemical compound Cl[Mn]Cl GLFNIEUTAYBVOC-UHFFFAOYSA-L 0.000 description 2
- 101100301239 Myxococcus xanthus recA1 gene Proteins 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 102100027378 Prothrombin Human genes 0.000 description 2
- 108010094028 Prothrombin Proteins 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 206010057190 Respiratory tract infections Diseases 0.000 description 2
- 238000012300 Sequence Analysis Methods 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- 241000191984 Staphylococcus haemolyticus Species 0.000 description 2
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 239000000556 agonist Substances 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 229940009098 aspartate Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000001110 calcium chloride Substances 0.000 description 2
- 229910001628 calcium chloride Inorganic materials 0.000 description 2
- 239000013592 cell lysate Substances 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 229920001436 collagen Polymers 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 239000006071 cream Substances 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 2
- SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 2
- SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 230000027948 extracellular matrix binding Effects 0.000 description 2
- 108010048325 fibrinopeptides gamma Proteins 0.000 description 2
- 244000144992 flock Species 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 125000001165 hydrophobic group Chemical group 0.000 description 2
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 238000002513 implantation Methods 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 230000002452 interceptive effect Effects 0.000 description 2
- 238000007918 intramuscular administration Methods 0.000 description 2
- 108020001756 ligand binding domains Proteins 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 239000011565 manganese chloride Substances 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 210000003205 muscle Anatomy 0.000 description 2
- 238000011587 new zealand white rabbit Methods 0.000 description 2
- 229910052759 nickel Inorganic materials 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 244000052769 pathogen Species 0.000 description 2
- 230000001717 pathogenic effect Effects 0.000 description 2
- 230000007170 pathology Effects 0.000 description 2
- 239000013600 plasmid vector Substances 0.000 description 2
- 229920001606 poly(lactic acid-co-glycolic acid) Polymers 0.000 description 2
- 108091033319 polynucleotide Proteins 0.000 description 2
- 102000040430 polynucleotide Human genes 0.000 description 2
- 239000002157 polynucleotide Substances 0.000 description 2
- 229920000136 polysorbate Polymers 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 238000000159 protein binding assay Methods 0.000 description 2
- 229940039716 prothrombin Drugs 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 150000003230 pyrimidines Chemical class 0.000 description 2
- 238000011552 rat model Methods 0.000 description 2
- 239000011541 reaction mixture Substances 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 201000009410 rhabdomyosarcoma Diseases 0.000 description 2
- 150000003384 small molecules Chemical class 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 210000002435 tendon Anatomy 0.000 description 2
- 230000005030 transcription termination Effects 0.000 description 2
- ALSTYHKOOCGGFT-KTKRTIGZSA-N (9Z)-octadecen-1-ol Chemical compound CCCCCCCC\C=C/CCCCCCCCO ALSTYHKOOCGGFT-KTKRTIGZSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 101150084750 1 gene Proteins 0.000 description 1
- WONRDHPFOHAWOG-UHFFFAOYSA-N 2-chloronaphthalen-1-ol Chemical compound C1=CC=C2C(O)=C(Cl)C=CC2=C1 WONRDHPFOHAWOG-UHFFFAOYSA-N 0.000 description 1
- NKDFYOWSKOHCCO-YPVLXUMRSA-N 20-hydroxyecdysone Chemical compound C1[C@@H](O)[C@@H](O)C[C@]2(C)[C@@H](CC[C@@]3([C@@H]([C@@](C)(O)[C@H](O)CCC(C)(O)C)CC[C@]33O)C)C3=CC(=O)[C@@H]21 NKDFYOWSKOHCCO-YPVLXUMRSA-N 0.000 description 1
- XMTQQYYKAHVGBJ-UHFFFAOYSA-N 3-(3,4-DICHLOROPHENYL)-1,1-DIMETHYLUREA Chemical compound CN(C)C(=O)NC1=CC=C(Cl)C(Cl)=C1 XMTQQYYKAHVGBJ-UHFFFAOYSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 1
- 108010042708 Acetylmuramyl-Alanyl-Isoglutamine Proteins 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 206010053555 Arthritis bacterial Diseases 0.000 description 1
- CZIVKMOEXPILDK-SRVKXCTJSA-N Asp-Tyr-Ser Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CO)C(O)=O CZIVKMOEXPILDK-SRVKXCTJSA-N 0.000 description 1
- 208000034309 Bacterial disease carrier Diseases 0.000 description 1
- 206010066798 Bacterial tracheitis Diseases 0.000 description 1
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
- 208000031462 Bovine Mastitis Diseases 0.000 description 1
- 208000004020 Brain Abscess Diseases 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 241000222122 Candida albicans Species 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 206010007882 Cellulitis Diseases 0.000 description 1
- 206010007918 Cellulitis orbital Diseases 0.000 description 1
- 101710198480 Clumping factor A Proteins 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 206010010741 Conjunctivitis Diseases 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 238000011537 Coomassie blue staining Methods 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical class OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
- 108010041986 DNA Vaccines Proteins 0.000 description 1
- 238000007399 DNA isolation Methods 0.000 description 1
- 229940021995 DNA vaccine Drugs 0.000 description 1
- 206010064687 Device related infection Diseases 0.000 description 1
- 206010012735 Diarrhoea Diseases 0.000 description 1
- BVTJGGGYKAMDBN-UHFFFAOYSA-N Dioxetane Chemical class C1COO1 BVTJGGGYKAMDBN-UHFFFAOYSA-N 0.000 description 1
- 206010014561 Emphysema Diseases 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 108050001049 Extracellular proteins Proteins 0.000 description 1
- 206010016936 Folliculitis Diseases 0.000 description 1
- 101150066516 GST gene Proteins 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 208000010412 Glaucoma Diseases 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 108010051815 Glutamyl endopeptidase Proteins 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 102000005720 Glutathione transferase Human genes 0.000 description 1
- 108010070675 Glutathione transferase Proteins 0.000 description 1
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 206010021531 Impetigo Diseases 0.000 description 1
- 208000004575 Infectious Arthritis Diseases 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- 108010085895 Laminin Proteins 0.000 description 1
- 102000007547 Laminin Human genes 0.000 description 1
- BMVFXOQHDQZAQU-DCAQKATOSA-N Leu-Pro-Asp Chemical compound CC(C)C[C@@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(=O)O)C(=O)O)N BMVFXOQHDQZAQU-DCAQKATOSA-N 0.000 description 1
- 206010024774 Localised infection Diseases 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- 102000043129 MHC class I family Human genes 0.000 description 1
- 108091054437 MHC class I family Proteins 0.000 description 1
- PWHULOQIROXLJO-UHFFFAOYSA-N Manganese Chemical compound [Mn] PWHULOQIROXLJO-UHFFFAOYSA-N 0.000 description 1
- 208000037942 Methicillin-resistant Staphylococcus aureus infection Diseases 0.000 description 1
- VVQNEPGJFQJSBK-UHFFFAOYSA-N Methyl methacrylate Chemical compound COC(=O)C(C)=C VVQNEPGJFQJSBK-UHFFFAOYSA-N 0.000 description 1
- MSFSPUZXLOGKHJ-UHFFFAOYSA-N Muraminsaeure Natural products OC(=O)C(C)OC1C(N)C(O)OC(CO)C1O MSFSPUZXLOGKHJ-UHFFFAOYSA-N 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 238000011887 Necropsy Methods 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
- 208000000493 Orbital Cellulitis Diseases 0.000 description 1
- 206010033078 Otitis media Diseases 0.000 description 1
- 108010078471 Panton-Valentine leukocidin Proteins 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 108010013639 Peptidoglycan Proteins 0.000 description 1
- 206010034531 Perinephric abscess Diseases 0.000 description 1
- 206010057182 Periorbital cellulitis Diseases 0.000 description 1
- 108010053210 Phycocyanin Proteins 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 102100038124 Plasminogen Human genes 0.000 description 1
- 108010051456 Plasminogen Proteins 0.000 description 1
- 239000004952 Polyamide Substances 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 229920001710 Polyorthoester Polymers 0.000 description 1
- MUPFEKGTMRGPLJ-RMMQSMQOSA-N Raffinose Natural products O(C[C@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O[C@@]2(CO)[C@H](O)[C@@H](O)[C@@H](CO)O2)O1)[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 MUPFEKGTMRGPLJ-RMMQSMQOSA-N 0.000 description 1
- 108091081062 Repeated sequence (DNA) Proteins 0.000 description 1
- 108700008625 Reporter Genes Proteins 0.000 description 1
- 206010038975 Retroperitoneal abscess Diseases 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 241000282849 Ruminantia Species 0.000 description 1
- 206010040070 Septic Shock Diseases 0.000 description 1
- 102100027287 Serpin H1 Human genes 0.000 description 1
- 108050008290 Serpin H1 Proteins 0.000 description 1
- 101000794214 Staphylococcus aureus Toxic shock syndrome toxin-1 Proteins 0.000 description 1
- 241000823609 Staphylococcus aureus subsp. aureus RN4220 Species 0.000 description 1
- 238000000692 Student's t-test Methods 0.000 description 1
- 208000002847 Surgical Wound Diseases 0.000 description 1
- 230000024932 T cell mediated immunity Effects 0.000 description 1
- 230000005867 T cell response Effects 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 108010034949 Thyroglobulin Proteins 0.000 description 1
- 102000009843 Thyroglobulin Human genes 0.000 description 1
- 206010044248 Toxic shock syndrome Diseases 0.000 description 1
- 231100000650 Toxic shock syndrome Toxicity 0.000 description 1
- MUPFEKGTMRGPLJ-UHFFFAOYSA-N UNPD196149 Natural products OC1C(O)C(CO)OC1(CO)OC1C(O)C(O)C(O)C(COC2C(C(O)C(O)C(CO)O2)O)O1 MUPFEKGTMRGPLJ-UHFFFAOYSA-N 0.000 description 1
- 206010046306 Upper respiratory tract infection Diseases 0.000 description 1
- 108010059993 Vancomycin Proteins 0.000 description 1
- 206010048038 Wound infection Diseases 0.000 description 1
- UZQJVUCHXGYFLQ-AYDHOLPZSA-N [(2s,3r,4s,5r,6r)-4-[(2s,3r,4s,5r,6r)-4-[(2r,3r,4s,5r,6r)-4-[(2s,3r,4s,5r,6r)-3,5-dihydroxy-6-(hydroxymethyl)-4-[(2s,3r,4s,5s,6r)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3,5-dihydroxy-6-(hy Chemical compound O([C@H]1[C@H](O)[C@@H](CO)O[C@H]([C@@H]1O)O[C@H]1[C@H](O)[C@@H](CO)O[C@H]([C@@H]1O)O[C@H]1CC[C@]2(C)[C@H]3CC=C4[C@@]([C@@]3(CC[C@H]2[C@@]1(C=O)C)C)(C)CC(O)[C@]1(CCC(CC14)(C)C)C(=O)O[C@H]1[C@@H]([C@@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O[C@H]4[C@@H]([C@@H](O[C@H]5[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O5)O)[C@H](O)[C@@H](CO)O4)O)[C@H](O)[C@@H](CO)O3)O)[C@H](O)[C@@H](CO)O2)O)[C@H](O)[C@@H](CO)O1)O)[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O UZQJVUCHXGYFLQ-AYDHOLPZSA-N 0.000 description 1
- 206010000269 abscess Diseases 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 208000013086 acute epiglottitis Diseases 0.000 description 1
- 230000001464 adherent effect Effects 0.000 description 1
- 239000000853 adhesive Substances 0.000 description 1
- 230000001070 adhesive effect Effects 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 239000007801 affinity label Substances 0.000 description 1
- 108010004469 allophycocyanin Proteins 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 229940037003 alum Drugs 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 229960003896 aminopterin Drugs 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000002399 angioplasty Methods 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 210000002159 anterior chamber Anatomy 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 208000029212 bacterial myositis Diseases 0.000 description 1
- 230000003385 bacteriostatic effect Effects 0.000 description 1
- 230000037429 base substitution Effects 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 229920002988 biodegradable polymer Polymers 0.000 description 1
- 239000004621 biodegradable polymer Substances 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 238000007413 biotinylation Methods 0.000 description 1
- 230000006287 biotinylation Effects 0.000 description 1
- 208000010217 blepharitis Diseases 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 239000006161 blood agar Substances 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 229940095731 candida albicans Drugs 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 125000002843 carboxylic acid group Chemical group 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 230000004709 cell invasion Effects 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 210000003169 central nervous system Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000002038 chemiluminescence detection Methods 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 230000035602 clotting Effects 0.000 description 1
- 238000000975 co-precipitation Methods 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 210000001072 colon Anatomy 0.000 description 1
- 230000006957 competitive inhibition Effects 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 230000001268 conjugating effect Effects 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 239000012050 conventional carrier Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 230000000139 costimulatory effect Effects 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 238000002716 delivery method Methods 0.000 description 1
- 210000000852 deltoid muscle Anatomy 0.000 description 1
- 239000004053 dental implant Substances 0.000 description 1
- 101150106284 deoR gene Proteins 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- VWLWTJHKQHRTNC-UHFFFAOYSA-L dipotassium;8-anilino-5-(4-anilino-5-sulfonatonaphthalen-1-yl)naphthalene-1-sulfonate Chemical compound [K+].[K+].C=12C(S(=O)(=O)[O-])=CC=CC2=C(C=2C3=CC=CC(=C3C(NC=3C=CC=CC=3)=CC=2)S([O-])(=O)=O)C=CC=1NC1=CC=CC=C1 VWLWTJHKQHRTNC-UHFFFAOYSA-L 0.000 description 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 239000006196 drop Substances 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 239000003221 ear drop Substances 0.000 description 1
- 229940047652 ear drops Drugs 0.000 description 1
- 238000001378 electrochemiluminescence detection Methods 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 239000003974 emollient agent Substances 0.000 description 1
- 206010014801 endophthalmitis Diseases 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 201000010063 epididymitis Diseases 0.000 description 1
- 208000001606 epiglottitis Diseases 0.000 description 1
- 229960003276 erythromycin Drugs 0.000 description 1
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000003889 eye drop Substances 0.000 description 1
- 229940012356 eye drops Drugs 0.000 description 1
- 230000001815 facial effect Effects 0.000 description 1
- 108091009104 fibrinogen binding proteins Proteins 0.000 description 1
- 102000036072 fibronectin binding proteins Human genes 0.000 description 1
- 108091010988 fibronectin binding proteins Proteins 0.000 description 1
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- 238000012921 fluorescence analysis Methods 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 238000001215 fluorescent labelling Methods 0.000 description 1
- 239000012737 fresh medium Substances 0.000 description 1
- 238000001730 gamma-ray spectroscopy Methods 0.000 description 1
- 230000002496 gastric effect Effects 0.000 description 1
- 238000012215 gene cloning Methods 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- 230000000322 hemodialysis Effects 0.000 description 1
- 230000028996 humoral immune response Effects 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000000521 hyperimmunizing effect Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000010820 immunofluorescence microscopy Methods 0.000 description 1
- 230000009851 immunogenic response Effects 0.000 description 1
- 229960001438 immunostimulant agent Drugs 0.000 description 1
- 239000003022 immunostimulating agent Substances 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 201000007119 infective endocarditis Diseases 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 210000001503 joint Anatomy 0.000 description 1
- 206010023332 keratitis Diseases 0.000 description 1
- 101150109249 lacI gene Proteins 0.000 description 1
- 210000000867 larynx Anatomy 0.000 description 1
- 238000013147 laser angioplasty Methods 0.000 description 1
- 239000004816 latex Substances 0.000 description 1
- 229920000126 latex Polymers 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 230000021633 leukocyte mediated immunity Effects 0.000 description 1
- 210000003041 ligament Anatomy 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 238000009630 liquid culture Methods 0.000 description 1
- 239000006210 lotion Substances 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 201000003453 lung abscess Diseases 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 229910052748 manganese Inorganic materials 0.000 description 1
- 239000011572 manganese Substances 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- MJGFBOZCAJSGQW-UHFFFAOYSA-N mercury sodium Chemical class [Na].[Hg] MJGFBOZCAJSGQW-UHFFFAOYSA-N 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- WSFSSNUMVMOOMR-NJFSPNSNSA-N methanone Chemical compound O=[14CH2] WSFSSNUMVMOOMR-NJFSPNSNSA-N 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 239000003094 microcapsule Substances 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 229940035032 monophosphoryl lipid a Drugs 0.000 description 1
- 239000002324 mouth wash Substances 0.000 description 1
- 229940051866 mouthwash Drugs 0.000 description 1
- 238000002887 multiple sequence alignment Methods 0.000 description 1
- BSOQXXWZTUDTEL-ZUYCGGNHSA-N muramyl dipeptide Chemical compound OC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)O[C@@H](O)[C@@H]1NC(C)=O BSOQXXWZTUDTEL-ZUYCGGNHSA-N 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 239000002105 nanoparticle Substances 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000010807 negative regulation of binding Effects 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 239000002674 ointment Substances 0.000 description 1
- 239000003883 ointment base Substances 0.000 description 1
- 229940055577 oleyl alcohol Drugs 0.000 description 1
- XMLQWXUVTXCDDL-UHFFFAOYSA-N oleyl alcohol Natural products CCCCCCC=CCCCCCCCCCCO XMLQWXUVTXCDDL-UHFFFAOYSA-N 0.000 description 1
- 239000002751 oligonucleotide probe Substances 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 238000012261 overproduction Methods 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 238000012335 pathological evaluation Methods 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- 230000010399 physical interaction Effects 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 229920000515 polycarbonate Polymers 0.000 description 1
- 239000004417 polycarbonate Substances 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920002635 polyurethane Polymers 0.000 description 1
- 239000004814 polyurethane Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 208000011354 prosthesis-related infectious disease Diseases 0.000 description 1
- 230000004952 protein activity Effects 0.000 description 1
- 239000003531 protein hydrolysate Substances 0.000 description 1
- 239000003725 proteoliposome Substances 0.000 description 1
- 239000001397 quillaja saponaria molina bark Substances 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- MUPFEKGTMRGPLJ-ZQSKZDJDSA-N raffinose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO[C@@H]2[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O2)O)O1 MUPFEKGTMRGPLJ-ZQSKZDJDSA-N 0.000 description 1
- 239000011535 reaction buffer Substances 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 208000020029 respiratory tract infectious disease Diseases 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000002207 retinal effect Effects 0.000 description 1
- 230000001177 retroviral effect Effects 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 239000012146 running buffer Substances 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 229930182490 saponin Natural products 0.000 description 1
- 150000007949 saponins Chemical class 0.000 description 1
- 238000003345 scintillation counting Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 201000009881 secretory diarrhea Diseases 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 201000001223 septic arthritis Diseases 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000011895 specific detection Methods 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 201000005789 splenic abscess Diseases 0.000 description 1
- 208000010110 spontaneous platelet aggregation Diseases 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 229920001059 synthetic polymer Polymers 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- MPLHNVLQVRSVEE-UHFFFAOYSA-N texas red Chemical compound [O-]S(=O)(=O)C1=CC(S(Cl)(=O)=O)=CC=C1C(C1=CC=2CCCN3CCCC(C=23)=C1O1)=C2C1=C(CCC1)C3=[N+]1CCCC3=C2 MPLHNVLQVRSVEE-UHFFFAOYSA-N 0.000 description 1
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 1
- 229940033663 thimerosal Drugs 0.000 description 1
- 108010061238 threonyl-glycine Proteins 0.000 description 1
- 230000002885 thrombogenetic effect Effects 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 229960002175 thyroglobulin Drugs 0.000 description 1
- 206010043778 thyroiditis Diseases 0.000 description 1
- 230000000451 tissue damage Effects 0.000 description 1
- 231100000827 tissue damage Toxicity 0.000 description 1
- 238000011200 topical administration Methods 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 239000012049 topical pharmaceutical composition Substances 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 231100000583 toxicological profile Toxicity 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000002463 transducing effect Effects 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- 239000001974 tryptic soy broth Substances 0.000 description 1
- 108010050327 trypticase-soy broth Proteins 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 230000002485 urinary effect Effects 0.000 description 1
- 210000001635 urinary tract Anatomy 0.000 description 1
- 229960003165 vancomycin Drugs 0.000 description 1
- MYPYJXKWCTUITO-LYRMYLQWSA-N vancomycin Chemical compound O([C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=C2C=C3C=C1OC1=CC=C(C=C1Cl)[C@@H](O)[C@H](C(N[C@@H](CC(N)=O)C(=O)N[C@H]3C(=O)N[C@H]1C(=O)N[C@H](C(N[C@@H](C3=CC(O)=CC(O)=C3C=3C(O)=CC=C1C=3)C(O)=O)=O)[C@H](O)C1=CC=C(C(=C1)Cl)O2)=O)NC(=O)[C@@H](CC(C)C)NC)[C@H]1C[C@](C)(N)[C@H](O)[C@H](C)O1 MYPYJXKWCTUITO-LYRMYLQWSA-N 0.000 description 1
- MYPYJXKWCTUITO-UHFFFAOYSA-N vancomycin Natural products O1C(C(=C2)Cl)=CC=C2C(O)C(C(NC(C2=CC(O)=CC(O)=C2C=2C(O)=CC=C3C=2)C(O)=O)=O)NC(=O)C3NC(=O)C2NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(CC(C)C)NC)C(O)C(C=C3Cl)=CC=C3OC3=CC2=CC1=C3OC1OC(CO)C(O)C(O)C1OC1CC(C)(N)C(O)C(C)O1 MYPYJXKWCTUITO-UHFFFAOYSA-N 0.000 description 1
- 230000002861 ventricular Effects 0.000 description 1
- 230000004580 weight loss Effects 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/305—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F)
- C07K14/31—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P15/00—Drugs for genital or sexual disorders; Contraceptives
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Physical Education & Sports Medicine (AREA)
- Cardiology (AREA)
- Genetics & Genomics (AREA)
- Heart & Thoracic Surgery (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Communicable Diseases (AREA)
- Rheumatology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Oncology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Endocrinology (AREA)
- Reproductive Health (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Materials For Medical Uses (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Claims (24)
- Isoliertes Nucleinsäuremolekül, das für ein Fibrinogen bindendes Protein kodiert, worin die Nucleinsäure für die Aminosäuresequenz von Seq.-ID Nr. 1 kodiert.
- Isolierte Nucleinsäure nach Anspruch 1, umfassend die Sequenz von Seq.-ID Nr. 2.
- Vektor, umfassend die isolierte Nucleinsäure nach Anspruch 1 oder Anspruch 2.
- Vektor nach Anspruch 3 in einem Mikroorganismus, der in der Lage ist, die Nucleinsäure zu exprimieren.
- Isoliertes Nucleinsäuremolekül nach Anspruch 1 oder Anspruch 2, kodierend für ein extrazelluläre Matrix bindendes Protein, das ein TYTFTDYVD-Motiv aufweist, worin das Protein von S. aureus isoliert und nicht ClfA ist.
- Vektor, der die isolierte Nucleinsäure nach Anspruch 5 umfasst.
- Vektor nach Anspruch 6 in einem Mikroorganismus, der in der Lage ist, die isolierte Nucleinsäure zu exprimieren.
- Isoliertes, rekombinantes oder synthetisches Protein, worin das Protein eine Aminosäuresequenz aufweist, die die Sequenz von Seq.-ID Nr. 1 umfasst.
- Protein nach Anspruch 8, für das eine Nucleinsäuresequenz kodiert, die die Sequenz von Seq.-ID Nr. 2 umfasst.
- Protein nach Anspruch 8, exprimiert von einem Vektor in einem lebenden Organismus, worin der Vektor eine Nucleinsäuresequenz enthält, die die Sequenz von Seq.-ID Nr. 2 umfasst.
- Isoliertes, rekombinantes oder synthetisches Protein nach Anspruch 8, das kationenabhängige Ligandenbindung aufweist und ein Consensus-TYTFTDYVD-Motiv aufweist, worin das Protein von S. aureus isoliert und nicht ClfA ist.
- Protein nach einem der Ansprüche 8 bis 11 in einem pharmazeutisch annehmbaren Träger.
- Protein nach Anspruch 12 in einem pharmazeutisch annehmbaren Träger.
- Protein nach einem der Ansprüche 8 bis 11, immobilisiert auf einer Festphase.
- Isolierter Antikörper oder isoliertes Antikörperfragment zur Sequenz TYTFTDYVD.
- Diagnoseset, umfassend ein Protein mit einer Aminosäuresequenz der Seq.-ID Nr. 1 oder ein Proteinfragment davon, das ein Consensus-TYTFTDYVD-Motiv aufweist, worin das Protein von S. aureus isoliert und nicht ClfA ist.
- Diagnoseset, umfassend einen Antikörper oder ein Antikörperfragment nach Anspruch 15.
- Protein nach einem der Ansprüche 8 bis 11 zur Verwendung bei der Behandlung einer S.-aureus-Infektion bei einem Patienten.
- Protein nach Anspruch 18, worin die Infektion Septikämie, Osteomyelitis, Mastitis oder Endocarditis ist.
- Protein nach einem der Ansprüche 8 bis 11 zur Verwendung in einem Verfahren zur Hemmung der Bindung von S. aureus an die extrazelluläre Matrix, um eine S.-aureus-Infektion bei einem Patienten zu behandeln oder ihr vorzubeugen.
- Wirksame Menge einer pharmazeutischen Zusammensetzung, die einen Antikörper oder ein Antikörperfragment nach Anspruch 15 umfasst, zur Verwendung in einem Verfahren zur Behandlung oder Prävention einer S.-aureus-Infektion bei einem Patienten.
- Zusammensetzung, umfassend ein Protein nach einem der Ansprüche 8 bis 11, zur Verwendung beim Überzug einer medizinischen Vorrichtung zum Reduzieren der S.-aureus-Infektion einer implantierten medizinischen Vorrichtung.
- Zusammensetzung nach Anspruch 22, worin die medizinische Vorrichtung aus der aus Gefäßtransplantaten, Gefäßstents, intravenösen Kathetern, künstlichen Herzklappen und Herzschrittmachern bestehenden Gruppe ausgewählt ist.
- Zusammensetzung, umfassend ein Protein nach einem der Ansprüche 8 bis 11, zur Verwendung als Impfstoff.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP10182690A EP2319931A1 (de) | 1997-11-26 | 1998-11-25 | Extrazellulären Matrix-bindende Proteine von Staphilococcus aureus |
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US6681597P | 1997-11-26 | 1997-11-26 | |
| US66815P | 1997-11-26 | ||
| US9842798P | 1998-08-31 | 1998-08-31 | |
| US98427P | 1998-08-31 | ||
| PCT/US1998/025246 WO1999027109A2 (en) | 1997-11-26 | 1998-11-25 | EXTRACELLULAR MATRIX-BINDING PROTEINS FROM $i(STAPHYLOCOCCUS AUREUS) |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP10182690.7 Division-Into | 2010-09-29 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EP1034277A2 EP1034277A2 (de) | 2000-09-13 |
| EP1034277B1 true EP1034277B1 (de) | 2012-06-27 |
Family
ID=26747174
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP98959613A Expired - Lifetime EP1034277B1 (de) | 1997-11-26 | 1998-11-25 | Extrazelluläre Matrix-bindende Proteine von Staphylococcus aureus |
| EP10182690A Withdrawn EP2319931A1 (de) | 1997-11-26 | 1998-11-25 | Extrazellulären Matrix-bindende Proteine von Staphilococcus aureus |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP10182690A Withdrawn EP2319931A1 (de) | 1997-11-26 | 1998-11-25 | Extrazellulären Matrix-bindende Proteine von Staphilococcus aureus |
Country Status (5)
| Country | Link |
|---|---|
| EP (2) | EP1034277B1 (de) |
| JP (2) | JP4486748B2 (de) |
| AU (1) | AU1537699A (de) |
| CA (1) | CA2310217A1 (de) |
| WO (1) | WO1999027109A2 (de) |
Families Citing this family (35)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6933366B2 (en) | 1996-12-27 | 2005-08-23 | Tripep Ab | Specificity exchangers that redirect antibodies to bacterial adhesion receptors |
| US6660842B1 (en) | 1994-04-28 | 2003-12-09 | Tripep Ab | Ligand/receptor specificity exchangers that redirect antibodies to receptors on a pathogen |
| DE69940404D1 (de) * | 1998-08-31 | 2009-03-26 | Inhibitex Inc | Multikomponenten Impfstoffe gegen Staphylococcus aureus |
| US6692739B1 (en) | 1998-08-31 | 2004-02-17 | Inhibitex, Inc. | Staphylococcal immunotherapeutics via donor selection and donor stimulation |
| EP1121149A4 (de) * | 1998-08-31 | 2002-03-20 | Inhibitex Inc | Immunotherapeutika gegen staphylokokkus mittels donor selektion und donor stimulation |
| MXPA01002120A (es) * | 1998-08-31 | 2003-03-27 | Trinity College Dublin | Polipeptidos y polinucleotidos de estafilococo negativo a coagulasa. |
| WO2002102829A2 (en) * | 2001-06-15 | 2002-12-27 | Inhibitex, Inc. | Cross-reactive monoclonal and polyclonal antibodies which recognize surface proteins from coagulase-negative staphylococci and staphylococcus aureus |
| US7335359B2 (en) | 2003-02-06 | 2008-02-26 | Tripep Ab | Glycosylated specificity exchangers |
| JP2007516157A (ja) | 2003-02-06 | 2007-06-21 | トリペップ アクチ ボラゲット | グリコシル化された抗原／抗体又はリガンド／受容体特異性交換体 |
| JP4836795B2 (ja) * | 2003-05-19 | 2011-12-14 | ブランデイズ ユニバーシティー | 核酸プロセシング方法、キット、及び装置 |
| WO2004110367A2 (en) * | 2003-05-29 | 2004-12-23 | Inhibitex, Inc. | Sdr proteins from staphylococcus capitis and their use in preventing and treating infections |
| ES2472441T3 (es) | 2004-09-22 | 2014-07-01 | Glaxosmithkline Biologicals S.A. | Composición inmunog�nica para uso en vacunación contra estafilococos |
| JP2009531387A (ja) | 2006-03-30 | 2009-09-03 | グラクソスミスクライン バイオロジカルズ ソシエテ アノニム | 免疫原性組成物 |
| WO2009029831A1 (en) | 2007-08-31 | 2009-03-05 | University Of Chicago | Methods and compositions related to immunizing against staphylococcal lung diseases and conditions |
| US9181329B2 (en) | 2007-08-31 | 2015-11-10 | The University Of Chicago | Methods and compositions related to immunizing against Staphylococcal lung diseases and conditions |
| US8466167B2 (en) | 2008-03-03 | 2013-06-18 | Irm Llc | Compounds and compositions as TLR activity modulators |
| WO2010014304A1 (en) | 2008-07-29 | 2010-02-04 | University Of Chicago | Compositions and methods related to staphylococcal bacterium proteins |
| HUE057713T2 (hu) | 2009-04-03 | 2022-05-28 | Univ Chicago | A protein A (SPA) variánsaival kapcsolatos készítmények és módszerek |
| CA2765112A1 (en) | 2009-06-10 | 2010-12-16 | Novartis Ag | Benzonaphthyridine-containing vaccines |
| SG10201406432RA (en) | 2009-06-22 | 2014-11-27 | Wyeth Llc | Compositions and methods for preparing staphylococcus aureus serotype 5 and 8 capsular polysaccharide conjugate immunogenic compositions |
| BRPI1015567A2 (pt) | 2009-06-22 | 2021-08-31 | Wyeth Llc | Composições imunogênicas de antígenos de staphylococcus aureus |
| GB0913680D0 (en) | 2009-08-05 | 2009-09-16 | Glaxosmithkline Biolog Sa | Immunogenic composition |
| JO3257B1 (ar) | 2009-09-02 | 2018-09-16 | Novartis Ag | مركبات وتركيبات كمعدلات لفاعلية tlr |
| ES2443952T3 (es) | 2009-09-02 | 2014-02-21 | Novartis Ag | Composiciones inmunógenas que incluyen moduladores de la actividad de TLR |
| WO2011057148A1 (en) | 2009-11-05 | 2011-05-12 | Irm Llc | Compounds and compositions as tlr-7 activity modulators |
| US9408907B2 (en) | 2009-12-15 | 2016-08-09 | Glaxosmithkline Biologicals Sa | Homogenous suspension of immunopotentiating compounds and uses thereof |
| EP2549990A1 (de) | 2010-03-23 | 2013-01-30 | Irm Llc | Verbindungen (cysteinbasierte lipopeptide) und zusammensetzungen als tlr2-agonisten zur behandlung von infektionen, entzündungen, atemwegserkrankungen etc. |
| WO2012003474A2 (en) | 2010-07-02 | 2012-01-05 | The University Of Chicago | Compositions and methods related to protein a (spa) variants |
| US9192661B2 (en) | 2010-07-06 | 2015-11-24 | Novartis Ag | Delivery of self-replicating RNA using biodegradable polymer particles |
| DK2654784T3 (en) | 2010-12-22 | 2017-02-13 | Wyeth Llc | STABLE IMMUNOGENIC COMPOSITIONS OF STAPHYLOCOCCUS AUREUS ANTIGENES |
| US8945588B2 (en) | 2011-05-06 | 2015-02-03 | The University Of Chicago | Methods and compositions involving protective staphylococcal antigens, such as EBH polypeptides |
| CN105188747A (zh) | 2013-02-01 | 2015-12-23 | 葛兰素史密斯克莱生物公司 | 包含toll样受体激动剂的免疫组合物的皮内递送 |
| KR101878529B1 (ko) * | 2014-09-25 | 2018-07-16 | 울산대학교 산학협력단 | 반코마이신 불균질 내성 황색포도알균 클론타입 판별용 바이오마커 조성물 및 이를 이용한 판별용 키트 |
| US11458151B2 (en) | 2018-02-12 | 2022-10-04 | Inimmune Corporation | Toll-like receptor ligands |
| CA3198924A1 (en) | 2020-11-04 | 2022-05-12 | Eligo Bioscience | Phage-derived particles for in situ delivery of dna payload into c. acnes population |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| ATE214942T1 (de) * | 1992-09-21 | 2002-04-15 | Alfa Laval Agri Internat Ab | Fibrinogen-bildungsprotein |
| EP0771351A1 (de) * | 1994-06-07 | 1997-05-07 | The Rockefeller University | Oberflächenprotein aus staphylococcus aureus |
| US6737248B2 (en) * | 1996-01-05 | 2004-05-18 | Human Genome Sciences, Inc. | Staphylococcus aureus polynucleotides and sequences |
| US5888971A (en) * | 1996-02-20 | 1999-03-30 | Ortho Pharmaceutical Corporation, Inc. | Macrocyclic peptides useful in the treatment of thrombin related disorders |
| SE9602496D0 (sv) * | 1996-06-20 | 1996-06-20 | Bengt Guss | Method and means for producing a fibrinogen binding protein and its use in biotechnology |
-
1998
- 1998-11-25 EP EP98959613A patent/EP1034277B1/de not_active Expired - Lifetime
- 1998-11-25 EP EP10182690A patent/EP2319931A1/de not_active Withdrawn
- 1998-11-25 CA CA002310217A patent/CA2310217A1/en not_active Abandoned
- 1998-11-25 JP JP2000522250A patent/JP4486748B2/ja not_active Expired - Fee Related
- 1998-11-25 WO PCT/US1998/025246 patent/WO1999027109A2/en active Application Filing
- 1998-11-25 AU AU15376/99A patent/AU1537699A/en not_active Abandoned
-
2010
- 2010-02-05 JP JP2010024144A patent/JP2010178737A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| AU1537699A (en) | 1999-06-15 |
| WO1999027109A3 (en) | 1999-09-02 |
| WO1999027109A2 (en) | 1999-06-03 |
| EP1034277A2 (de) | 2000-09-13 |
| JP4486748B2 (ja) | 2010-06-23 |
| CA2310217A1 (en) | 1999-06-03 |
| EP2319931A1 (de) | 2011-05-11 |
| JP2010178737A (ja) | 2010-08-19 |
| JP2002505075A (ja) | 2002-02-19 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EP1034277B1 (de) | Extrazelluläre Matrix-bindende Proteine von Staphylococcus aureus | |
| US7834151B2 (en) | SDRD protein from Staphylococcus aureus and diagnostic kits including same | |
| EP1117772B1 (de) | Polypeptide und polynukleotide aus coagulase-negativen staphylokokken | |
| KR20010085745A (ko) | 다성분 백신 | |
| US7638135B2 (en) | Collagen-binding proteins from enterococcal bacteria | |
| US20020169288A1 (en) | Collagen-binding adhesin from staphylococcus epidermidis and method of use | |
| EP1173466A1 (de) | Verfahren zur vermeidung der bindung von leukozyten an fibrinogen | |
| US20040038327A1 (en) | Antibodies to polypeptides from coagulase-negative staphylococci | |
| CA2503110A1 (en) | Collagen-binding proteins from enterococcal bacteria | |
| AU2004203421B2 (en) | Polypeptides and polynucleotides from coagulase-negative staphylococci |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PUAI | Public reference made under article 153(3) epc to a published international application that has entered the european phase |
Free format text: ORIGINAL CODE: 0009012 |
|
| 17P | Request for examination filed |
Effective date: 20000615 |
|
| AK | Designated contracting states |
Kind code of ref document: A2 Designated state(s): AT BE CH CY DE DK ES FI FR GB GR IE IT LI LU MC NL PT SE |
|
| 17Q | First examination report despatched |
Effective date: 20031016 |
|
| RTI1 | Title (correction) |
Free format text: EXTRACELLULAR MATRIX-BINDING PROTEINS FROM STAPHYLOCOCCUS AUREUS |
|
| GRAP | Despatch of communication of intention to grant a patent |
Free format text: ORIGINAL CODE: EPIDOSNIGR1 |
|
| GRAJ | Information related to disapproval of communication of intention to grant by the applicant or resumption of examination proceedings by the epo deleted |
Free format text: ORIGINAL CODE: EPIDOSDIGR1 |
|
| GRAP | Despatch of communication of intention to grant a patent |
Free format text: ORIGINAL CODE: EPIDOSNIGR1 |
|
| GRAC | Information related to communication of intention to grant a patent modified |
Free format text: ORIGINAL CODE: EPIDOSCIGR1 |
|
| GRAS | Grant fee paid |
Free format text: ORIGINAL CODE: EPIDOSNIGR3 |
|
| GRAA | (expected) grant |
Free format text: ORIGINAL CODE: 0009210 |
|
| AK | Designated contracting states |
Kind code of ref document: B1 Designated state(s): AT BE CH CY DE DK ES FI FR GB GR IE IT LI LU MC NL PT SE |
|
| REG | Reference to a national code |
Ref country code: GB Ref legal event code: FG4D |
|
| REG | Reference to a national code |
Ref country code: CH Ref legal event code: EP |
|
| REG | Reference to a national code |
Ref country code: AT Ref legal event code: REF Ref document number: 564270 Country of ref document: AT Kind code of ref document: T Effective date: 20120715 |
|
| REG | Reference to a national code |
Ref country code: IE Ref legal event code: FG4D |
|
| REG | Reference to a national code |
Ref country code: DE Ref legal event code: R096 Ref document number: 69842780 Country of ref document: DE Effective date: 20120823 |
|
| PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: FI Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20120627 |
|
| REG | Reference to a national code |
Ref country code: NL Ref legal event code: VDEP Effective date: 20120627 |
|
| REG | Reference to a national code |
Ref country code: AT Ref legal event code: MK05 Ref document number: 564270 Country of ref document: AT Kind code of ref document: T Effective date: 20120627 |
|
| PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: GR Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20120928 |
|
| PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: CY Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20120627 Ref country code: AT Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20120627 Ref country code: BE Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20120627 |
|
| PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: IT Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20120627 Ref country code: PT Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20121029 |
|
| PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: NL Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20120627 |
|
| PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: ES Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20121008 Ref country code: DK Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20120627 |
|
| PLBE | No opposition filed within time limit |
Free format text: ORIGINAL CODE: 0009261 |
|
| STAA | Information on the status of an ep patent application or granted ep patent |
Free format text: STATUS: NO OPPOSITION FILED WITHIN TIME LIMIT |
|
| REG | Reference to a national code |
Ref country code: DE Ref legal event code: R119 Ref document number: 69842780 Country of ref document: DE |
|
| 26N | No opposition filed |
Effective date: 20130328 |
|
| REG | Reference to a national code |
Ref country code: CH Ref legal event code: PL |
|
| GBPC | Gb: european patent ceased through non-payment of renewal fee |
Effective date: 20121125 |
|
| REG | Reference to a national code |
Ref country code: DE Ref legal event code: R097 Ref document number: 69842780 Country of ref document: DE Effective date: 20130328 |
|
| PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: LI Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20121130 Ref country code: CH Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20121130 |
|
| REG | Reference to a national code |
Ref country code: FR Ref legal event code: ST Effective date: 20130731 |
|
| REG | Reference to a national code |
Ref country code: IE Ref legal event code: MM4A |
|
| REG | Reference to a national code |
Ref country code: DE Ref legal event code: R119 Ref document number: 69842780 Country of ref document: DE Effective date: 20130601 |
|
| PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: IE Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20121125 Ref country code: DE Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20130601 |
|
| PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: FR Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20121130 Ref country code: GB Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20121125 |
|
| PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: MC Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20121130 |
|
| PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: LU Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20121125 |
|
| PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: SE Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20120627 |